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T‐cell antigen‐receptor stoichiometry: pre‐clustering for sensitivity
Author(s) -
Alarcón Balbino,
Swamy Mahima,
van Santen Hisse M,
Schamel Wolfgang W A
Publication year - 2006
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400682
Subject(s) - t cell receptor , receptor , cd3 , antigen , biology , ligand (biochemistry) , protein subunit , t cell , microbiology and biotechnology , biophysics , immune system , biochemistry , chemistry , immunology , cd8 , gene
The T‐cell antigen receptor (TCR˙CD3) is a multi‐subunit complex that is responsible for triggering an adaptive immune response. It shows high specificity and sensitivity, while having a low affinity for the ligand. Furthermore, T cells respond to antigen over a wide concentration range. The stoichiometry and architecture of TCR˙CD3 in the membrane have been under intense scrutiny because they might be the key to explaining its paradoxical properties. This review highlights new evidence that TCR˙CD3 is found on intact unstimulated T cells in a monovalent form (one ligand‐binding site per receptor) as well as in several distinct multivalent forms. This is in contrast to the TCR˙CD3 stoichiometries determined by several biochemical means; however, these data can be explained by the effects of different detergents on the integrity of the receptor. Here, we discuss a model in which the multivalent receptors are important for the detection of low concentrations of ligand and therefore confer sensitivity, whereas the co‐expressed monovalent TCR˙CD3s allow a wide dynamic range.